Derek Parsonage to Escherichia coli
This is a "connection" page, showing publications Derek Parsonage has written about Escherichia coli.
Connection Strength
0.697
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Parsonage D, Sheng F, Hirata K, Debnath A, McKerrow JH, Reed SL, Abagyan R, Poole LB, Podust LM. X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action. J Struct Biol. 2016 May; 194(2):180-90.
Score: 0.129
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Parsonage D, Miller H, Ross RP, Claiborne A. Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli. J Biol Chem. 1993 Feb 15; 268(5):3161-7.
Score: 0.105
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Reeves SA, Parsonage D, Nelson KJ, Poole LB. Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin. Biochemistry. 2011 Oct 18; 50(41):8970-81.
Score: 0.095
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Parsonage D, Reeves SA, Karplus PA, Poole LB. Engineering of fluorescent reporters into redox domains to monitor electron transfers. Methods Enzymol. 2010; 474:1-21.
Score: 0.087
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Parsonage D, Al-Shawi MK, Senior AE. Directed mutations of the strongly conserved lysine 155 in the catalytic nucleotide-binding domain of beta-subunit of F1-ATPase from Escherichia coli. J Biol Chem. 1988 Apr 05; 263(10):4740-4.
Score: 0.075
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Parsonage D, Luba J, Mallett TC, Claiborne A. The soluble alpha-glycerophosphate oxidase from Enterococcus casseliflavus. Sequence homology with the membrane-associated dehydrogenase and kinetic analysis of the recombinant enzyme. J Biol Chem. 1998 Sep 11; 273(37):23812-22.
Score: 0.039
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Claiborne A, Ross RP, Parsonage D. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Trends Biochem Sci. 1992 May; 17(5):183-6.
Score: 0.025
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al-Shawi MK, Parsonage D, Senior AE. Adenosine triphosphatase and nucleotide binding activity of isolated beta-subunit preparations from Escherichia coli F1F0-ATP synthase. J Biol Chem. 1990 Apr 05; 265(10):5595-601.
Score: 0.022
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al-Shawi MK, Parsonage D, Senior AE. Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPases. J Biol Chem. 1990 Mar 15; 265(8):4402-10.
Score: 0.021
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al-Shawi MK, Parsonage D, Senior AE. Kinetic characterization of the unisite catalytic pathway of seven beta-subunit mutant F1-ATPases from Escherichia coli. J Biol Chem. 1989 Sep 15; 264(26):15376-83.
Score: 0.021
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Kironde FA, Parsonage D, Senior AE. Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli. Biochem J. 1989 Apr 15; 259(2):421-6.
Score: 0.020
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Al-Shawi MK, Parsonage D, Senior AE. Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase. J Biol Chem. 1988 Dec 25; 263(36):19633-9.
Score: 0.020
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Maggio MB, Parsonage D, Senior AE. A mutation in the alpha-subunit of F1-ATPase from Escherichia coli affects the binding of F1 to the membrane. J Biol Chem. 1988 Apr 05; 263(10):4619-23.
Score: 0.019
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Lee MH, Nittayajarn A, Ross RP, Rothschild CB, Parsonage D, Claiborne A, Rubens CE. Characterization of Enterococcus faecalis alkaline phosphatase and use in identifying Streptococcus agalactiae secreted proteins. J Bacteriol. 1999 Sep; 181(18):5790-9.
Score: 0.010
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Crane EJ, Parsonage D, Claiborne A. The active-site histidine-10 of enterococcal NADH peroxidase is not essential for catalytic activity. Biochemistry. 1996 Feb 20; 35(7):2380-7.
Score: 0.008